SAC31_MOUSE
ID SAC31_MOUSE Reviewed; 427 AA.
AC A6H687; B7ZMU9; Q8BVY1; Q9QXE1;
DT 23-OCT-2007, integrated into UniProtKB/Swiss-Prot.
DT 24-JUL-2007, sequence version 1.
DT 25-MAY-2022, entry version 79.
DE RecName: Full=SAC3 domain-containing protein 1;
DE AltName: Full=SAC3 homology domain-containing protein 1;
GN Name=Sac3d1; Synonyms=Shd1;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, TISSUE SPECIFICITY, AND SUBCELLULAR
RP LOCATION.
RC STRAIN=C57BL/6J;
RX PubMed=15322101; DOI=10.1074/jbc.m405347200;
RA Khuda S.E., Yoshida M., Xing Y., Shimasaki T., Takeya M., Kuwahara K.,
RA Sakaguchi N.;
RT "The Sac3 homologue shd1 is involved in mitotic progression in mammalian
RT cells.";
RL J. Biol. Chem. 279:46182-46190(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 15-427.
RC STRAIN=C57BL/6J;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
CC -!- FUNCTION: Involved in centrosome duplication and mitotic progression.
CC {ECO:0000269|PubMed:15322101}.
CC -!- SUBUNIT: May be part of a SEM1-containing complex. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, microtubule organizing
CC center, centrosome {ECO:0000269|PubMed:15322101}. Cytoplasm,
CC cytoskeleton, spindle {ECO:0000269|PubMed:15322101}. Note=Localizes on
CC centrosomes in interphase cells and at spindles in mitosis.
CC -!- TISSUE SPECIFICITY: Present in spleen cells (at protein level).
CC {ECO:0000269|PubMed:15322101}.
CC -!- SIMILARITY: Belongs to the SAC3 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAC36061.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AJ131957; CAB65242.2; -; mRNA.
DR EMBL; BC144812; AAI44813.1; -; mRNA.
DR EMBL; BC145789; AAI45790.1; -; mRNA.
DR EMBL; AK075930; BAC36061.1; ALT_INIT; mRNA.
DR CCDS; CCDS37896.1; -.
DR RefSeq; NP_598439.3; NM_133678.3.
DR AlphaFoldDB; A6H687; -.
DR SMR; A6H687; -.
DR BioGRID; 211450; 1.
DR STRING; 10090.ENSMUSP00000109161; -.
DR iPTMnet; A6H687; -.
DR PhosphoSitePlus; A6H687; -.
DR EPD; A6H687; -.
DR MaxQB; A6H687; -.
DR PaxDb; A6H687; -.
DR PeptideAtlas; A6H687; -.
DR PRIDE; A6H687; -.
DR ProteomicsDB; 255452; -.
DR GeneID; 66406; -.
DR KEGG; mmu:66406; -.
DR CTD; 29901; -.
DR MGI; MGI:1913656; Sac3d1.
DR eggNOG; KOG1860; Eukaryota.
DR InParanoid; A6H687; -.
DR OrthoDB; 1410585at2759; -.
DR PhylomeDB; A6H687; -.
DR BioGRID-ORCS; 66406; 2 hits in 75 CRISPR screens.
DR PRO; PR:A6H687; -.
DR Proteomes; UP000000589; Unplaced.
DR RNAct; A6H687; protein.
DR GO; GO:0005813; C:centrosome; IDA:MGI.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR GO; GO:0015630; C:microtubule cytoskeleton; IDA:MGI.
DR GO; GO:0005634; C:nucleus; IDA:MGI.
DR GO; GO:0005819; C:spindle; IDA:MGI.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR GO; GO:0051298; P:centrosome duplication; IMP:MGI.
DR GO; GO:0046426; P:negative regulation of receptor signaling pathway via JAK-STAT; IDA:MGI.
DR GO; GO:0050776; P:regulation of immune response; IMP:MGI.
DR GO; GO:0051225; P:spindle assembly; IMP:MGI.
DR InterPro; IPR000717; PCI_dom.
DR InterPro; IPR045107; SAC3/GANP/THP3.
DR InterPro; IPR005062; SAC3/GANP/THP3_conserved.
DR PANTHER; PTHR12436; PTHR12436; 1.
DR Pfam; PF03399; SAC3_GANP; 1.
DR PROSITE; PS50250; PCI; 1.
PE 1: Evidence at protein level;
KW Cell cycle; Cell division; Cytoplasm; Cytoskeleton; Mitosis;
KW Phosphoprotein; Reference proteome.
FT CHAIN 1..427
FT /note="SAC3 domain-containing protein 1"
FT /id="PRO_0000308205"
FT DOMAIN 229..397
FT /note="PCI"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01185"
FT REGION 1..53
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 101..143
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 425
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:A6NKF1"
FT CONFLICT 49
FT /note="Q -> R (in Ref. 1; CAB65242)"
FT /evidence="ECO:0000305"
FT CONFLICT 266..276
FT /note="VEALQEVLQLP -> LEAPAGGST (in Ref. 1; CAB65242)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 427 AA; 46384 MW; 99C5F943CCD935AE CRC64;
MGRFKGENRS QARWIMGGVS KGRGSGKSRK PRQAAFGQTG ARVCPSSPQQ DAVPRFRWPG
DAECASSTHT PTMSGCKLPM GLCPDMCPAA ERARRERERR LHRLEVEPGG RGNAPRADPK
RTVKEYSRPA AGKPRPPPSL LRPPPVLLAT VRYLAGEVAG RGDVSCAEVA SFVADRLRAV
RLDLSLQGVD DADAATVLEA ALATLLAVVA RVRPEETRGA ADPVLLQTQV QEGFGSLRRC
YARGKGPYPR QAAFQGLFLL YNLGSVEALQ EVLQLPAALR ACPPLQAALA VDAAFREDNH
ARLFRLLRTL PYLQSCAVQE HIGYARRKAL ARLSRALSTP KGQTLPLDFI EHFLALDGLQ
EARDLCQAHG LTLDKDRVVF LRGQYSEEGL PPPGAYHILV GNKLQGHTLE DVVMAEEGDI
HRPGSAA
